ID   GCH1L_CHLTR             Reviewed;         251 AA.
AC   O84110;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN   OrderedLocusNames=CT_108;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P0AFP6}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC       {ECO:0000305}.
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DR   EMBL; AE001273; AAC67699.1; -; Genomic_DNA.
DR   PIR; C71557; C71557.
DR   RefSeq; NP_219611.1; NC_000117.1.
DR   RefSeq; WP_009871455.1; NC_000117.1.
DR   AlphaFoldDB; O84110; -.
DR   SMR; O84110; -.
DR   STRING; 813.O172_00585; -.
DR   EnsemblBacteria; AAC67699; AAC67699; CT_108.
DR   GeneID; 884109; -.
DR   KEGG; ctr:CT_108; -.
DR   PATRIC; fig|272561.5.peg.118; -.
DR   HOGENOM; CLU_037423_3_0_0; -.
DR   InParanoid; O84110; -.
DR   OMA; HGLFWRG; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002678; DUF34/NIF3.
DR   InterPro; IPR036069; DUF34/NIF3_sf.
DR   PANTHER; PTHR13799; PTHR13799; 1.
DR   Pfam; PF01784; NIF3; 1.
DR   SUPFAM; SSF102705; SSF102705; 1.
DR   TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..251
FT                   /note="GTP cyclohydrolase 1 type 2 homolog"
FT                   /id="PRO_0000147303"
FT   BINDING         64
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         65
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         102
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         219
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         223
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT   BINDING         223
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0AFP6"
SQ   SEQUENCE   251 AA;  27474 MW;  A4C2F6BE7517298E CRC64;
     MNVSDLLNIL NELLHPEYFS DYGPNGLQVG NAQTAIRKVA VAVTADLATI EKAIACEANV
     LLVHHGIFWK GMPYSITGIL YQRMQRLMEG NIQLIAYHLP LDAHTTIGNN WKVARDLGWE
     QLESFGSSQP SLGVKGVFPE MEVHDFISQL SAYYQTPVLA KALGGKKRVS SAALISGGAY
     REISEAKNQQ VDCFITGNFD EPAWSLAHEL AIHFLAFGHT ATEKVGPKAL AQYLKGAGLE
     SVVFLDTDNP F